Gene Rv2626c
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Function unknown |
| Product | Hypoxic response protein 1 Hrp1 |
| Comments | Rv2626c, (MTCY01A10.06), len: 143 aa. Hrp1, hypoxic response protein 1, similar to CAC49670|SMB21441 putative inosine-5'-monophosphate dehydrogenase protein from Rhizobium meliloti (Sinorhizobium meliloti) (120 aa), FASTA scores: opt: 287, E(): 6.6e-12, (43.75% identity in 112 aa overlap) (has its N-terminus shorter 27 aa); AAK78655|CAC0678 CBS domains from Clostridium acetobutylicum (142 aa), FASTA scores: opt: 276, E(): 3.9e-11, (35.65% identity in 115 aa overlap); Q9K9P0|BH2605 BH2605 protein from Bacillus halodurans (142 aa), FASTA scores: opt: 276, E(): 3.9e-11, (35.65% identity in 115 aa overlap); etc. Also some similarity to P71737|Rv2406c|MTCY253.14 hypothetical 15.1 KDA protein from Mycobacterium tuberculosis (142 aa), FASTA scores: opt: 145, E(): 0.00012, (22.3% identity in 112 aa overlap). Predicted possible vaccine candidate (See Zvi et al., 2008). |
| Functional category | Conserved hypotheticals |
| Proteomics | The product of this CDS corresponds to spot 2626c identified in cell wall by proteomics at the Statens Serum Institute (Denmark), and at the Max Planck Institute for Infection Biology, Berlin, Germany (see proteomics citations). Identified in immunodominant fractions of M. tuberculosis H37Rv cytosol using 2D-LPE, 2D-PAGE, and LC-MS or LC-MS/MS (See Covert et al., 2001). Also identified at the Statens Serum Institute (Denmark) under aerobic and low oxygen conditions (see Rosenkrands et al., 2002). Identified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in the culture supernatant of M. tuberculosis H37Rv using mass spectrometry (See Mattow et al., 2003). Identified in the cytosol of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the membrane protein fraction and whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate (See de Souza et al., 2011). |
| Transcriptomics | mRNA identified by DNA microarray analysis (gene induced by hypoxia) (see Sherman et al., 2001). DNA microarrays show increased expression in M. tuberculosis H37Rv in BALB/c mice compared to SCID mice, after 21 days of infection (See Talaat et al., 2004). DNA microarrays and qRT-PCR indicate regulation by MprA under physiological conditions and environmental stress (SDS and Triton X-100) (See He et al., 2006). |
| Mutant | Non-essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Non-essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Non-essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 2952562 | 2952993 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2626c|hrp1
MTTARDIMNAGVTCVGEHETLTAAAQYMREHDIGALPICGDDDRLHGMLTDRDIVIKGLAAGLDPNTATAGELARDSIYYVDANASIQEMLNVMEEHQVRRVPVISEHRLVGIVTEADIARHLPEHAIVQFVKAICSPMALAS
Bibliography
- Jungblut PR, Schaible UE, Mollenkopf HJ, Zimny-Arndt U, Raupach B, Mattow J, Halada P, Lamer S, Hagens K and Kaufmann SH [1999]. Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens. Proteomics
- Rosenkrands I et al. [2000]. Towards the proteome of Mycobacterium tuberculosis. Proteomics
- Rosenkrands I, Weldingh K, Jacobsen S, Hansen CV, Florio W, Gianetri I and Andersen P [2000]. Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection. Proteomics
- Sherman DR, Voskuil M, Schnappinger D, Liao R, Harrell MI and Schoolnik GK [2001]. Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding alpha -crystallin. Transcriptome
- Covert BA et al. [2001]. The application of proteomics in defining the T cell antigens of Mycobacterium tuberculosis. Proteomics
- Rosenkrands I et al. [2002]. Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins. Proteomics Regulation
- Park HD et al. [2003]. Rv3133c/dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosis. Transcriptome
- Voskuil MI, Schnappinger D, Visconti KC, Harrell MI, Dolganov GM, Sherman DR and Schoolnik GK [2003]. Inhibition of respiration by nitric oxide induces a Mycobacterium tuberculosis dormancy program. Regulon
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Proteomics
- Mattow J, Schaible UE, Schmidt F, Hagens K, Siejak F, Brestrich G, Haeselbarth G, Muller EC, Jungblut PR and Kaufmann SH [2003]. Comparative proteome analysis of culture supernatant proteins from virulent Mycobacterium tuberculosis H37Rv and attenuated M. bovis BCG Copenhagen. Proteomics
- Talaat AM et al. [2004]. The temporal expression profile of Mycobacterium tuberculosis infection in mice. Transcriptome
- Sharpe ML et al. [2005]. Crystallization of a protein using dehydration without a precipitant. Product Structure
- Mawuenyega KG et al. [2005]. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Proteomics
- He H et al. [2006]. MprAB is a stress-responsive two-component system that directly regulates expression of sigma factors SigB and SigE in Mycobacterium tuberculosis. Regulation Transcriptome
- Sharpe ML et al. [2008]. The structure and unusual protein chemistry of hypoxic response protein 1, a latency antigen and highly expressed member of the DosR regulon in Mycobacterium tuberculosis. Structure
- Zvi A et al. [2008]. Whole genome identification of Mycobacterium tuberculosis vaccine candidates by comprehensive data mining and bioinformatic analyses. Immunology
- Målen H et al. [2010]. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv. Proteomics
- Griffin JE et al. [2011]. High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism. Mutant
- de Souza GA et al. [2011]. Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway. Proteomics
- Mazandu GK et al. [2012]. Function prediction and analysis of mycobacterium tuberculosis hypothetical proteins. Function
- DeJesus MA et al. [2017]. Comprehensive Essentiality Analysis of the Mycobacterium tuberculosis Genome via Saturating Transposon Mutagenesis. Mutant
- Minato Y et al. [2019]. Genomewide Assessment of Mycobacterium tuberculosis Conditionally Essential Metabolic Pathways. Mutant
